ID A0A0S6VZ99_9BACT Unreviewed; 1183 AA.
AC A0A0S6VZ99;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Pyruvate-flavodoxin oxidoreductase {ECO:0000313|EMBL:GAK50995.1};
GN ORFNames=U14_02237 {ECO:0000313|EMBL:GAK50995.1};
OS Candidatus Moduliflexus flocculans.
OC Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK50995.1};
RN [1] {ECO:0000313|EMBL:GAK50995.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA Hugenholtz P.;
RT "First genomic representation of candidate bacterial phylum KSB3 points to
RT enhanced environmental sensing as a trigger of wastewater bulking.";
RL PeerJ 3:e740-e740(2015).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRSR:PIRSR000159-50};
CC Note=Binds 3 [4Fe-4S] clusters per subunit.
CC {ECO:0000256|PIRSR:PIRSR000159-50};
CC -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009032,
CC ECO:0000256|PIRNR:PIRNR000159}.
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DR EMBL; DF820456; GAK50995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S6VZ99; -.
DR STRING; 1499966.U14_02237; -.
DR HOGENOM; CLU_002569_0_0_0; -.
DR Proteomes; UP000030700; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR CDD; cd03377; TPP_PFOR_PNO; 1.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 4.10.780.10; Pyruvate-flavodoxin oxidoreductase, EKR domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR037112; Pyrv-flavodox_OxR_EKR_sf.
DR InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR011895; Pyrv_flavodox_OxRed.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR02176; pyruv_ox_red; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF10371; EKR; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR PIRSF; PIRSF000159; NifJ; 1.
DR SMART; SM00890; EKR; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR000159-50};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000159};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000159-50};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000159-
KW 50};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000159-50};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000159}; Pyruvate {ECO:0000313|EMBL:GAK50995.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030700};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000159}.
FT DOMAIN 683..712
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 739..770
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 34
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 67
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 117
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 692
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 695
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 698
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 702
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 748
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 751
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 754
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 758
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 815
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 818
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 820
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 843
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT BINDING 843
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 972..975
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1001..1006
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-1"
FT BINDING 1081
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-50"
FT SITE 34
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 67
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 117
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
FT SITE 1006
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000159-2"
SQ SEQUENCE 1183 AA; 129363 MW; 2ADE80E245ABCFE5 CRC64;
MSNTVKDVRT IDGNTAAAYV SYAFSDVAAL YPITPSSVMG ETADEMRAKG TKNIFGQKVK
IVEMQSEAGA AGAVHGSLTG GALTTTYTAS QGLLLMIPNM YKIAGELLPA VFHVSARAVA
AHALSIFGDH SDVMATRQIG WTLLASANNQ EVIDLGTVAH LSAIQSRVPV LHFFDGFRTS
HELSKVEMIP YEDLAKLVDM DAIKAFKARG FRPEKPEMRG TAQNPDIFFQ AKEAVNPFYT
NLPDILEANM KKVAELTGRT YNLFDYVGAP DAECVIISMG SSVDVIEETI NYLNAKGAKL
GVIKVRVYRP WSAKHLLAAI PASVKKIAVL DRCKEAGSVG EPLYEDVLSC FYEVGKKDVM
VIGGRYGLSS KEFTPAMVKA VYDNLDSVSP KNHFTVGITD DVSFTSLDVK ETFVTEPEGT
ICCKFWGLGS DGTVGANKNS IKIIGDHTDM YAQGYFSYDS KKSGGVTVSH LRFGPKEINS
HYLITESDFI ACHNQSYITR LDVLEGIKQG GAFLLNCVWS PEELSEKLPP AVKRTLAQKN
VDFYIINAYK IAEEIGLGHR INMVLQAAFF KISKVISDYE KALEYMRDAV KKTYGKKGDT
VVAMNVAAVN RGADELVKIT IPADWATAKD EADTTVYPND FVRDVLNPIN AQKGDLLPSS
RFAPDGIFPT GMTQYEKRGI AVNVPKWVAE NCIQCNQCSL VCPHAVVRPY LLTADEAAKV
PAGTPLADAK GKELAGYKYK IQISPLDCTG CGSCSDVCPA KEKALVMTPL EDLVEQESTQ
YAYLKTLPVK DQLMSKFSLK GSQFRQPLFE FSGACAGCGE TPYVKLITQM FGERMVVANA
TGCSSIYGGT APVSPYTTNK DGYGPSWANS LFEDNAEYGL GMYLGISQTR DKLILLAEEA
RSFKLDGELS GALESWLNNY SNADESVKLS QVIKAKLPAA VESASGREKE VLAEMLEKQD
YFAKKSVWIF GGDGWAYDIG YGGLDHVIAS GLDVNILVLD TEVYSNTGGQ ASKASQTGQI
AKFAATGKEQ CKKDLGMMAM SYGYVYVASV SMGANMNQTL KAFQEAEAYP GPSLLICYSP
CINHGINMTH SINEAKRAVQ SGYWPLYRYN PVLKNEGKNP FVFESKDPDG SFQDFLKSEV
RYSALKKMYP EIAEKAFAKA ERDMMGRYKY YKKLSEIDFS DMV
//
